1br4

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(New page: 200px<br /><applet load="1br4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1br4, resolution 3.62&Aring;" /> '''SMOOTH MUSCLE MYOSIN...)
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[[Image:1br4.gif|left|200px]]<br /><applet load="1br4" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1br4.gif|left|200px]]<br /><applet load="1br4" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1br4, resolution 3.62&Aring;" />
caption="1br4, resolution 3.62&Aring;" />
'''SMOOTH MUSCLE MYOSIN MOTOR DOMAIN-ESSENTIAL LIGHT CHAIN COMPLEX WITH MGADP.BEF3 BOUND AT THE ACTIVE SITE'''<br />
'''SMOOTH MUSCLE MYOSIN MOTOR DOMAIN-ESSENTIAL LIGHT CHAIN COMPLEX WITH MGADP.BEF3 BOUND AT THE ACTIVE SITE'''<br />
==Overview==
==Overview==
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The crystal structures of an expressed vertebrate smooth muscle myosin, motor domain (MD) and a motor domain-essential light chain (ELC) complex, (MDE), both with a transition state analog (MgADP x AIF4-) in the active, site, have been determined to 2.9 A and 3.5 A resolution, respectively., The MDE structure with an ATP analog (MgADP x BeFx) was also determined to, 3.6 A resolution. In all three structures, a domain of the C-terminal, region, the "converter," is rotated approximately 70 degrees from that in, nucleotide-free skeletal subfragment 1 (S1). We have found that the, MDE-BeFx and MDE-AIF4- structures are almost identical, consistent with, the fact that they both bind weakly to actin. A comparison of the lever, arm positions in MDE-AIF4- and in nucleotide-free skeletal S1 shows that a, potential displacement of approximately 10 nm can be achieved during the, power stroke.
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The crystal structures of an expressed vertebrate smooth muscle myosin motor domain (MD) and a motor domain-essential light chain (ELC) complex (MDE), both with a transition state analog (MgADP x AIF4-) in the active site, have been determined to 2.9 A and 3.5 A resolution, respectively. The MDE structure with an ATP analog (MgADP x BeFx) was also determined to 3.6 A resolution. In all three structures, a domain of the C-terminal region, the "converter," is rotated approximately 70 degrees from that in nucleotide-free skeletal subfragment 1 (S1). We have found that the MDE-BeFx and MDE-AIF4- structures are almost identical, consistent with the fact that they both bind weakly to actin. A comparison of the lever arm positions in MDE-AIF4- and in nucleotide-free skeletal S1 shows that a potential displacement of approximately 10 nm can be achieved during the power stroke.
==About this Structure==
==About this Structure==
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1BR4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with MG, ADP and BEF as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Myosin_ATPase Myosin ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.1 3.6.4.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BR4 OCA].
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1BR4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=BEF:'>BEF</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Myosin_ATPase Myosin ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.1 3.6.4.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BR4 OCA].
==Reference==
==Reference==
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[[Category: Cohen, C.]]
[[Category: Cohen, C.]]
[[Category: Dominguez, R.]]
[[Category: Dominguez, R.]]
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[[Category: Trybus, K.M.]]
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[[Category: Trybus, K M.]]
[[Category: ADP]]
[[Category: ADP]]
[[Category: BEF]]
[[Category: BEF]]
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[[Category: muscle protein]]
[[Category: muscle protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:51:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:12 2008''

Revision as of 09:58, 21 February 2008

Image:1br4.gif

1br4, resolution 3.62Å

Drag the structure with the mouse to rotate

SMOOTH MUSCLE MYOSIN MOTOR DOMAIN-ESSENTIAL LIGHT CHAIN COMPLEX WITH MGADP.BEF3 BOUND AT THE ACTIVE SITE

Overview

The crystal structures of an expressed vertebrate smooth muscle myosin motor domain (MD) and a motor domain-essential light chain (ELC) complex (MDE), both with a transition state analog (MgADP x AIF4-) in the active site, have been determined to 2.9 A and 3.5 A resolution, respectively. The MDE structure with an ATP analog (MgADP x BeFx) was also determined to 3.6 A resolution. In all three structures, a domain of the C-terminal region, the "converter," is rotated approximately 70 degrees from that in nucleotide-free skeletal subfragment 1 (S1). We have found that the MDE-BeFx and MDE-AIF4- structures are almost identical, consistent with the fact that they both bind weakly to actin. A comparison of the lever arm positions in MDE-AIF4- and in nucleotide-free skeletal S1 shows that a potential displacement of approximately 10 nm can be achieved during the power stroke.

About this Structure

1BR4 is a Protein complex structure of sequences from Gallus gallus with , and as ligands. Active as Myosin ATPase, with EC number 3.6.4.1 Full crystallographic information is available from OCA.

Reference

Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state., Dominguez R, Freyzon Y, Trybus KM, Cohen C, Cell. 1998 Sep 4;94(5):559-71. PMID:9741621

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